Purification of some glycoside hydrolases by affinity chromatography

Two glycoproteins have been isolated from the cell walls of baker's yeast. One is a glucan-protein complex which has been partially characterised as having a branched carbohydrate structure composed of chains of (1 leads to 3)-linked beta-D-glucosyl residues, some of which are attached by (1 leads to 6)-linkages to the main chain. Immobilization of this glycoprotein was achieved by covalent attachment to Sepharose, and the product was used to isolate a number of (1 leads to 3)-beta-D-glucan hydrolases from Helix pomatia, malted barley, and Basidiomycete QM806. The second glycoprotein, a mannan-protein complex, after immobilization, has been used in the purification of an alpha-D-mannosidase from jack-bean meal.